Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00337
Entry Name
UniProt Accession
Theoretical PI
5.36
Molecular Weight
99530.1
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
Protein Synonyms/Alias
GMP-PDE alpha; 3.1.4.35;
Gene Name
Pde6a
Gene Synonyms/Alias
Mpa; Pdea;
Created Date
01-AUG-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
856
Canonical
GAPASKSCCIQ****
[1]
S-Farnesylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Qin N, Pittler SJ, Baehr W. In vitro isoprenylation and membrane associationof mouse rod photoreceptor cGMP phosphodiesterase alpha and beta subunitsexpressed in bacteria. J Biol Chem. 1992 Apr 25;267(12):8458-63.[PMID:1314827]
Functional Description
This protein participates in processes of transmission and amplification of the visual signal.
Sequence Annotation
Domain: 73 222 GAF 1.
Domain: 254 431 GAF 2.
Active site: 559 559 Proton donor.
Metal binding site: 563 563 Divalent metal cation 1.
Metal binding site: 599 599 Divalent metal cation 1.
Metal binding site: 600 600 Divalent metal cation 1.
Metal binding site: 600 600 Divalent metal cation 2.
Metal binding site: 720 720 Divalent metal cation 1.
Modified residue: 2 2 N-acetylglycine.
Modified residue: 856 856 Cysteine methyl ester.
Protein Length
859 AA.
Protein Sequence
(Canonical)
MGEVTAEEVE KFLDSNIGFA KQYYNFHYRG KVISDLLGAK EAAVDFSNYH DVNSVEESEI  60
IFDLLRDVQE NLQAEKCTFN VMKKLCFLLR ADRMSLFMYR TRNGIAELAT RLFNVHKDAV  120
LEDCLVMPDS EIVFPLDMGV VGHVAHSKKI ANVPNTEEDE HFCDFVDNLT EYQTKNILAS  180
PIMNGKDVVA IIMAVNKIDE PHFTKRDEEI LLKYLNFVNL IMKVFHLSYL HNCETRRGQI  240
LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP  300
AYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPADHW ALVSGLPTYV AQNGLICNIM  360
NAPAEDFFEF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDDMDETLM  420
ESLTQFLGWS VLNPDTYESM NKLENRKDIF QDIVKYHVKC DNEEIQKILK TREVYGKEPW  480
ECEEEELAEI LQGELPDAES YEINKFHFSD LPLTELELVK CGIQMYYELR VVDKFHIPQE  540
ALVRFMYSLS KGYRRITYHN WRHGFNVGQT MFSLLVTGKL KRYFTDLEAL AMVTAAFCHD  600
IDHRGTNNLY QMKSQNPLAK LHGSSILERH HLEFGKTLLR DESLNIFQNL NRRQHEHAIH  660
MMDIAIIATD LALYFKKRTM FQKIVDQSKT YESTQEWTQY MMLEQTRKEI VMAMMMTACD  720
LSAITKPWEV QSKVALLVAA EFWEQGDLER TVLQQNPIPM MDRNKADELP KLQVGFIDFV  780
CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYEAKM KALEEEKQKQ QAAKQAASGN  840
QPGGNPLQGA PASKSCCIQ                                               859
FASTA
(Canonical)
>LipidDB-10090-00337|P27664
MGEVTAEEVEKFLDSNIGFAKQYYNFHYRGKVISDLLGAKEAAVDFSNYHDVNSVEESEI
IFDLLRDVQENLQAEKCTFNVMKKLCFLLRADRMSLFMYRTRNGIAELATRLFNVHKDAV
LEDCLVMPDSEIVFPLDMGVVGHVAHSKKIANVPNTEEDEHFCDFVDNLTEYQTKNILAS
PIMNGKDVVAIIMAVNKIDEPHFTKRDEEILLKYLNFVNLIMKVFHLSYLHNCETRRGQI
LLWSGSKVFEELTDIERQFHKALYTVRAFLNCDRYSVGLLDMTKQKEFFDVWPVLMGEAP
AYSGPRTPDGREINFYKVIDYILHGKEDIKVIPNPPADHWALVSGLPTYVAQNGLICNIM
NAPAEDFFEFQKEPLDESGWMIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDDMDETLM
ESLTQFLGWSVLNPDTYESMNKLENRKDIFQDIVKYHVKCDNEEIQKILKTREVYGKEPW
ECEEEELAEILQGELPDAESYEINKFHFSDLPLTELELVKCGIQMYYELRVVDKFHIPQE
ALVRFMYSLSKGYRRITYHNWRHGFNVGQTMFSLLVTGKLKRYFTDLEALAMVTAAFCHD
IDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKTLLRDESLNIFQNLNRRQHEHAIH
MMDIAIIATDLALYFKKRTMFQKIVDQSKTYESTQEWTQYMMLEQTRKEIVMAMMMTACD
LSAITKPWEVQSKVALLVAAEFWEQGDLERTVLQQNPIPMMDRNKADELPKLQVGFIDFV
CTFVYKEFSRFHEEITPMLDGITNNRKEWKALADEYEAKMKALEEEKQKQQAAKQAASGN
QPGGNPLQGAPASKSCCIQ
Gene Ontology
GO:0005886; C:plasma membrane; TAS:Reactome
GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:UniProtKB-EC
GO:0046872; F:metal ion binding; IEA:UniProtKB-KW
GO:0060041; P:retina development in camera-type eye; IMP:MGI
GO:0007165; P:signal transduction; IEA:InterPro
GO:0007601; P:visual perception; IEA:UniProtKB-KW
Interpro
InterPro; IPR003018; GAF
InterPro; IPR029016; GAF_dom_like
InterPro; IPR003607; HD/PDEase_dom
InterPro; IPR023088; PDEase
InterPro; IPR002073; PDEase_catalytic_dom
InterPro; IPR023174; PDEase_CS
Pfam
Pfam; PF01590; GAF;
Pfam; PF00233; PDEase_I;
SMART
SMART; SM00065; GAF;
SMART; SM00471; HDc;
PROSITE
PROSITE; PS00126; PDEASE_I;
PRINTS
PRINTS; PR00387; PDIESTERASE1;